2025
Rapid folding of nascent RNA regulates eukaryotic RNA biogenesis
Schärfen L, Vock I, Simon M, Neugebauer K. Rapid folding of nascent RNA regulates eukaryotic RNA biogenesis. Molecular Cell 2025, 85: 1561-1574.e5. PMID: 40139190, PMCID: PMC12009195, DOI: 10.1016/j.molcel.2025.02.025.Peer-Reviewed Original ResearchConceptsRibosome biogenesisBase pairsNascent pre-mRNACo-transcriptional foldingRNA processing eventsRNA base pairsRDNA lociNascent RNARNA biogenesisRNA polymerasePol IIRRNA nucleotidesNascent chainsPol ICoding PotentialPairing statusPre-mRNAMature mRNABase-paired stateElongating ribosomeFunctional conformationProcessing eventsBiogenesisRibosomeNucleotide
2021
An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel
Urrutia J, Aguado A, Gomis-Perez C, Muguruza-Montero A, Ballesteros OR, Zhang J, Nuñez E, Malo C, Chung HJ, Leonardo A, Bergara A, Villarroel A. An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel. BMC Biology 2021, 19: 109. PMID: 34020651, PMCID: PMC8138981, DOI: 10.1186/s12915-021-01040-1.Peer-Reviewed Original ResearchConceptsKv7.2 channelsChannel functionSequences of proteinsNon-native configurationsNascent chainsProper foldingEpilepsy-causing mutationsIQ motifResponsive domainHuman diseasesHelix ANative conformationFolding routeIon channelsKCNQ2 geneMutationsNeuronal compartmentsFoldingMisfoldingProteinKey pathogenic mechanismsPathogenic variantsSilico studiesPathogenic mechanismsSide chains
1994
Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane.
Mothes W, Prehn S, Rapoport T. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. The EMBO Journal 1994, 13: 3973-3982. PMID: 8076593, PMCID: PMC395317, DOI: 10.1002/j.1460-2075.1994.tb06713.x.Peer-Reviewed Original ResearchMeSH KeywordsAffinity LabelsAmino Acid SequenceAzirinesBenzoatesBiological TransportCell CompartmentationCross-Linking ReagentsDNA Mutational AnalysisEndoplasmic ReticulumLysineMembrane ProteinsModels, BiologicalMolecular Sequence DataProlactinProtein BiosynthesisProtein PrecursorsSEC Translocation ChannelsStructure-Activity RelationshipUltraviolet RaysConceptsSec61 alphaNascent chainsProtein interactsSignal sequenceProtein-conducting channelSecretory protein preprolactinNascent polypeptide chainsEndoplasmic reticulum membranePhoto-crosslinking approachSec61p complexER membraneMembrane proteinsMembrane environmentSecretory proteinsPolypeptide segmentsReticulum membranePolypeptide chainTranslocation processHydrophobic coreRibosomesProtein environmentProteinTranslocationPhotoreactive groupSequence
1977
5′-Terminal nucleotide sequences of polio virus polyribosomal RNA and virion RNA are identical
PETTERSSON R, FLANEGAN J, ROSE J, BALTIMORE D. 5′-Terminal nucleotide sequences of polio virus polyribosomal RNA and virion RNA are identical. Nature 1977, 268: 270-272. PMID: 196211, DOI: 10.1038/268270a0.Peer-Reviewed Original ResearchConceptsVirion RNAPolyribosomal RNANucleotide sequenceInitiation of RNAPositive-strand virusesNucleotide sequence relationshipsNascent chainsRNA moleculesRNA chainsPositive strandSequence relationshipsRNANegative strandProteinReplicative intermediatesPoliovirion RNAA-GpViral RNAMRNAVirus RNASequenceStrandsTerminusCells3Virus
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply